ID A0A1M6HQQ1_9ACTN Unreviewed; 757 AA.
AC A0A1M6HQQ1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Formate acetyltransferase {ECO:0000256|RuleBase:RU368075};
DE EC=2.3.1.54 {ECO:0000256|RuleBase:RU368075};
DE AltName: Full=Pyruvate formate-lyase {ECO:0000256|RuleBase:RU368075};
GN ORFNames=SAMN02745244_02031 {ECO:0000313|EMBL:SHJ24414.1};
OS Tessaracoccus bendigoensis DSM 12906.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=1123357 {ECO:0000313|EMBL:SHJ24414.1, ECO:0000313|Proteomes:UP000184512};
RN [1] {ECO:0000313|EMBL:SHJ24414.1, ECO:0000313|Proteomes:UP000184512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12906 {ECO:0000313|EMBL:SHJ24414.1,
RC ECO:0000313|Proteomes:UP000184512};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + formate = CoA + pyruvate; Xref=Rhea:RHEA:11844,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15740, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.1.54;
CC Evidence={ECO:0000256|ARBA:ARBA00001179,
CC ECO:0000256|RuleBase:RU368075};
CC -!- PATHWAY: Fermentation; pyruvate fermentation; formate from pyruvate:
CC step 1/1. {ECO:0000256|RuleBase:RU368075}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU368075}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU368075}.
CC -!- SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family. PFL
CC subfamily. {ECO:0000256|ARBA:ARBA00008375,
CC ECO:0000256|RuleBase:RU368075}.
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DR EMBL; FQZG01000034; SHJ24414.1; -; Genomic_DNA.
DR RefSeq; WP_073187815.1; NZ_FQZG01000034.1.
DR AlphaFoldDB; A0A1M6HQQ1; -.
DR STRING; 1123357.SAMN02745244_02031; -.
DR OrthoDB; 9803969at2; -.
DR UniPathway; UPA00920; UER00891.
DR Proteomes; UP000184512; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008861; F:formate C-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01678; PFL1; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR005949; Form_AcTrfase.
DR InterPro; IPR019777; Form_AcTrfase_GR_CS.
DR InterPro; IPR001150; Gly_radical.
DR InterPro; IPR004184; PFL_dom.
DR NCBIfam; TIGR01255; pyr_form_ly_1; 1.
DR PANTHER; PTHR30191; FORMATE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR30191:SF0; FORMATE ACETYLTRANSFERASE 1; 1.
DR Pfam; PF01228; Gly_radical; 1.
DR Pfam; PF02901; PFL-like; 1.
DR PIRSF; PIRSF000379; For_Ac_trans_1; 1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR PROSITE; PS00850; GLY_RADICAL_1; 1.
DR PROSITE; PS51149; GLY_RADICAL_2; 1.
DR PROSITE; PS51554; PFL; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU368075};
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU368075};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU368075};
KW Glucose metabolism {ECO:0000256|RuleBase:RU368075};
KW Organic radical {ECO:0000256|ARBA:ARBA00022818,
KW ECO:0000256|PIRSR:PIRSR000379-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000184512};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368075}.
FT DOMAIN 7..627
FT /note="PFL"
FT /evidence="ECO:0000259|PROSITE:PS51554"
FT DOMAIN 634..757
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT ACT_SITE 420
FT /note="S-acetylcysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT ACT_SITE 421
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-1"
FT MOD_RES 732
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 757 AA; 83617 MW; 9F471C157DE83D0D CRC64;
MTASAPTREE SLVPEDPWGG FVPGAWSNSI DVRDFILTNF TPYDGDASFL AGPTAKTLGV
WETLQRDYLS VERTKRIYDV ETHIPGDVDA FPAGYISSDD DVIVGLQTDT PLKRPMMPAG
GWRMVETATR EAGLEPDPRI KEIFTRYRKT HNEAVFDIYT PRIRAARSSH LVTGLPDAYG
RGRIIGDYRR VALYGVDALI AAKQTDKDSV ADQPFSEDWA RYREEHSEQI KALKKLKNLG
ASYGFDLSRP AATFHEAVQW TYLAYLASVK SQDGAAMSIG RLSGFFDIYA QRDLASGLIT
ESDAQEIIDA LVTKLRIVRF LRTIDYDQIF SGDPYWATWS DGGFANDGRT LVTKTSFRLL
QTLRNLGPAP EPNITIYWDA KLPEGYKAFC ASISIETSAI QYESDAEIRN QWGDDTAIAC
CVSPMAIGKQ MQFFGARLNT AKALLYAING GRDEMSGKQI IDGYEPITGD EPLDFDTVWA
KYDAMLDHAV HTYVEALNII HYSHDKYAYE AMEMALHDDE IVRTMGCGMA GLSIVADSLA
AIKYATVTPV RDETGLVVDY ITEGDFPMYG NDDDRADELA KLVVSTVMGK IRKIKLYRDA
VPTQSVLTIT SNVVYGKATG AFPSGHEAGT PFAPGANPEN GADTHGMLAS MMSVGKLEYE
DALDGISLTN TITPTALGRT EEERIANLVG ILDAGMGEGL YHANINVLNR ETLLDAMENP
ENYPQLTIRV SGYAVNFVKL TREQQLDVLS RTFHEAL
//
